Abstract
We show that a two-step process, involving spontaneous self-assembly of lipids and apolipoproteins and surface patterning, produces single, supported lipid bilayers over two discrete and independently adjustable length scales. Specifically, an aqueous phase incubation of DMPC vesicles with purified apolipoprotein A-I results in the reconstitution of high density lipoprotein (rHDL), wherein nanoscale clusters of single lipid bilayers are corralled by the protein. Adsorption of these discoidal particles to clean hydrophilic glass (or silicon) followed by direct exposure to a spatial pattern of short-wavelength UV radiation directly produces microscopic patterns of nanostructured bilayers. Alternatively, simple incubation of aqueous phase rHDL with a chemically patterned hydrophilic/hydrophobic surface produces a novel compositional pattern, caused by an increased affinity for adsorption onto hydrophilic regions relative to the surrounding hydrophobic regions. Further, by simple chemical denaturation of the boundary protein, nanoscale compartmentalization can be selectively erased, thus producing patterns of laterally fluid, lipid bilayers structured solely at the mesoscopic length scale. Since these aqueous phase microarrays of nanostructured lipid bilayers allow for membrane proteins to be embedded within single nanoscale bilayer compartments, they present a viable means of generating high-density membrane protein arrays. Such a system would permit in-depth elucidation of membrane protein structure-function relationships and the consequences of membrane compartmentalization on lipid dynamics.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 11164-11169 |
| Number of pages | 6 |
| Journal | Journal of the American Chemical Society |
| Volume | 130 |
| Issue number | 33 |
| DOIs | |
| State | Published - Aug 20 2008 |
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ASJC Scopus subject areas
- Chemistry(all)
Cite this
Bridging across length scales : Multi-scale ordering of supported lipid bilayers via lipoprotein self-assembly and surface patterning. / Vinchurkar, Madhuri S.; Bricarello, Daniel A.; Lagerstedt, Jens O.; Buban, James P.; Stahlberg, Henning; Oda, Michael N.; Voss, John C; Parikh, Atul N.
In: Journal of the American Chemical Society, Vol. 130, No. 33, 20.08.2008, p. 11164-11169.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Bridging across length scales
T2 - Multi-scale ordering of supported lipid bilayers via lipoprotein self-assembly and surface patterning
AU - Vinchurkar, Madhuri S.
AU - Bricarello, Daniel A.
AU - Lagerstedt, Jens O.
AU - Buban, James P.
AU - Stahlberg, Henning
AU - Oda, Michael N.
AU - Voss, John C
AU - Parikh, Atul N.
PY - 2008/8/20
Y1 - 2008/8/20
N2 - We show that a two-step process, involving spontaneous self-assembly of lipids and apolipoproteins and surface patterning, produces single, supported lipid bilayers over two discrete and independently adjustable length scales. Specifically, an aqueous phase incubation of DMPC vesicles with purified apolipoprotein A-I results in the reconstitution of high density lipoprotein (rHDL), wherein nanoscale clusters of single lipid bilayers are corralled by the protein. Adsorption of these discoidal particles to clean hydrophilic glass (or silicon) followed by direct exposure to a spatial pattern of short-wavelength UV radiation directly produces microscopic patterns of nanostructured bilayers. Alternatively, simple incubation of aqueous phase rHDL with a chemically patterned hydrophilic/hydrophobic surface produces a novel compositional pattern, caused by an increased affinity for adsorption onto hydrophilic regions relative to the surrounding hydrophobic regions. Further, by simple chemical denaturation of the boundary protein, nanoscale compartmentalization can be selectively erased, thus producing patterns of laterally fluid, lipid bilayers structured solely at the mesoscopic length scale. Since these aqueous phase microarrays of nanostructured lipid bilayers allow for membrane proteins to be embedded within single nanoscale bilayer compartments, they present a viable means of generating high-density membrane protein arrays. Such a system would permit in-depth elucidation of membrane protein structure-function relationships and the consequences of membrane compartmentalization on lipid dynamics.
AB - We show that a two-step process, involving spontaneous self-assembly of lipids and apolipoproteins and surface patterning, produces single, supported lipid bilayers over two discrete and independently adjustable length scales. Specifically, an aqueous phase incubation of DMPC vesicles with purified apolipoprotein A-I results in the reconstitution of high density lipoprotein (rHDL), wherein nanoscale clusters of single lipid bilayers are corralled by the protein. Adsorption of these discoidal particles to clean hydrophilic glass (or silicon) followed by direct exposure to a spatial pattern of short-wavelength UV radiation directly produces microscopic patterns of nanostructured bilayers. Alternatively, simple incubation of aqueous phase rHDL with a chemically patterned hydrophilic/hydrophobic surface produces a novel compositional pattern, caused by an increased affinity for adsorption onto hydrophilic regions relative to the surrounding hydrophobic regions. Further, by simple chemical denaturation of the boundary protein, nanoscale compartmentalization can be selectively erased, thus producing patterns of laterally fluid, lipid bilayers structured solely at the mesoscopic length scale. Since these aqueous phase microarrays of nanostructured lipid bilayers allow for membrane proteins to be embedded within single nanoscale bilayer compartments, they present a viable means of generating high-density membrane protein arrays. Such a system would permit in-depth elucidation of membrane protein structure-function relationships and the consequences of membrane compartmentalization on lipid dynamics.
UR - http://www.scopus.com/inward/record.url?scp=50249084457&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=50249084457&partnerID=8YFLogxK
U2 - 10.1021/ja803110v
DO - 10.1021/ja803110v
M3 - Article
C2 - 18642906
AN - SCOPUS:50249084457
VL - 130
SP - 11164
EP - 11169
JO - Journal of the American Chemical Society
JF - Journal of the American Chemical Society
SN - 0002-7863
IS - 33
ER -